메뉴 건너뛰기




Volumn 421, Issue 6924, 2003, Pages 756-760

Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; CRYSTAL STRUCTURE; MONOCLONAL ANTIBODIES; ONCOLOGY; TISSUE; TUMORS;

EID: 0037434791     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01392     Document Type: Article
Times cited : (1331)

References (30)
  • 2
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • Olayioye, M. A., Neve, R. M., Lane, H. A. & Hynes, N. E. The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J. 19, 3159-3167 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 3
    • 0000701437 scopus 로고    scopus 로고
    • ed. O'Malley, B. W. Academic, San Diego
    • Tang, C. K. & Lippman, M. E. in Hormones and Signaling (ed. O'Malley, B. W.) 113-165 (Academic, San Diego, 1998).
    • (1998) Hormones and Signaling , pp. 113-165
    • Tang, C.K.1    Lippman, M.E.2
  • 4
    • 37049183697 scopus 로고
    • Human breast cancer: Correlation of relapse and survival with amplification of the HER-2/neu oncogene
    • Slamon, D. J. et al. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 235, 177-182 (1987).
    • (1987) Science , vol.235 , pp. 177-182
    • Slamon, D.J.1
  • 5
    • 0035869407 scopus 로고    scopus 로고
    • Use of chemotherapy plus a monoclonal antibody against HER 2 for metastatic breast cancer that overexpress HER2
    • Slamon, D. J. et al. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpress HER2. N. Engl. J. Med. 344, 783-792 (2001).
    • (2001) N. Engl. J. Med. , vol.344 , pp. 783-792
    • Slamon, D.J.1
  • 6
    • 0023082137 scopus 로고
    • Receptors for epidermal growth factor and other polypeptide mitogens
    • Carpenter, G. Receptors for epidermal growth factor and other polypeptide mitogens. Annu. Rev. Biochem. 56, 881-914 (1987).
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 881-914
    • Carpenter, G.1
  • 7
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 103, 211-225 (2000).
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 8
    • 0033009389 scopus 로고    scopus 로고
    • Binding specificities and affinities of egf domains for ErbB receptors
    • Jones, J. T., Akita, R. W. & Sliwkowski, M. X. Binding specificities and affinities of egf domains for ErbB receptors. FEBS Lett. 447, 227-231 (1999).
    • (1999) FEBS Lett. , vol.447 , pp. 227-231
    • Jones, J.T.1    Akita, R.W.2    Sliwkowski, M.X.3
  • 9
    • 0023196582 scopus 로고
    • erbB-2 is a potent oncogene when overexpressed in NIH/3T3 cells
    • Di Fiore, P. P. et al. erbB-2 is a potent oncogene when overexpressed in NIH/3T3 cells. Science 237, 178-182 (1987).
    • (1987) Science , vol.237 , pp. 178-182
    • Di Fiore, P.P.1
  • 10
    • 18644386251 scopus 로고    scopus 로고
    • Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
    • Ogiso, H. et al. Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell 110, 775-787 (2002).
    • (2002) Cell , vol.110 , pp. 775-787
    • Ogiso, H.1
  • 11
    • 18644370411 scopus 로고    scopus 로고
    • Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor α
    • Garrett, T. P. J. et al. Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor α. Cell 110, 763-773 (2002).
    • (2002) Cell , vol.110 , pp. 763-773
    • Garrett, T.P.J.1
  • 12
    • 0013381656 scopus 로고    scopus 로고
    • EGF activates its receptor by relieving auto-inhibition of ectodomain dimerization
    • in the press
    • Ferguson, K. M. et al. EGF activates its receptor by relieving auto-inhibition of ectodomain dimerization. Mol. Cell (in the press).
    • Mol. Cell
    • Ferguson, K.M.1
  • 13
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Cho, H. S. & Leahy, D. J. Structure of the extracellular region of HER3 reveals an interdomain tether. Science 297, 1330-1333 (2002).
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.S.1    Leahy, D.J.2
  • 14
    • 0031253786 scopus 로고    scopus 로고
    • VL:VH domain rotations in engineered antibodies: Crystal structures of the Fab fragments from two murine antitumor antibodies and their engineered human constructs
    • Banfield, M. J., King, D. J., Mountain, A. & Brady, R. L. VL:VH domain rotations in engineered antibodies: crystal structures of the Fab fragments from two murine antitumor antibodies and their engineered human constructs. Proteins 29, 161-171 (1997).
    • (1997) Proteins , vol.29 , pp. 161-171
    • Banfield, M.J.1    King, D.J.2    Mountain, A.3    Brady, R.L.4
  • 15
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence, M. C. & Colman, P. M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946-950 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 16
    • 0037008698 scopus 로고    scopus 로고
    • Disabling receptor ensembles with rationally designed interface peptidomimetics
    • Berezov, A. et al. Disabling receptor ensembles with rationally designed interface peptidomimetics. J. Biol. Chem. 277, 28330-28339 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 28330-28339
    • Berezov, A.1
  • 17
    • 0034638925 scopus 로고    scopus 로고
    • Molecular mechanisms underlying ErbB2/HER2 action in breast cancer
    • Harari, D. & Yarden, Y. Molecular mechanisms underlying ErbB2/HER2 action in breast cancer. Oncogene 19, 6102-6114 (2000).
    • (2000) Oncogene , vol.19 , pp. 6102-6114
    • Harari, D.1    Yarden, Y.2
  • 18
    • 0032851961 scopus 로고    scopus 로고
    • Nonclinical studies addressing the mechanism of action of Trastuzumab (Herceptin)
    • Sliwkowski, M. X. et al. Nonclinical studies addressing the mechanism of action of Trastuzumab (Herceptin). Semin. Oncol. 26, 60-70 (1999).
    • (1999) Semin. Oncol. , vol.26 , pp. 60-70
    • Sliwkowski, M.X.1
  • 19
    • 0035874981 scopus 로고    scopus 로고
    • Trastuzumab (Herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ectodomain cleavage in breast cancer cells
    • Molina, M. A. et al. Trastuzumab (Herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ectodomain cleavage in breast cancer cells. Cancer Res. 61, 4744-4749 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 4744-4749
    • Molina, M.A.1
  • 20
    • 0030614530 scopus 로고    scopus 로고
    • Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation
    • Burke, C. L., Lemmon, M. A., Coren, B. A., Engelman, D. M. & Stern, D. F. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene 14, 687-696 (1997).
    • (1997) Oncogene , vol.14 , pp. 687-696
    • Burke, C.L.1    Lemmon, M.A.2    Coren, B.A.3    Engelman, D.M.4    Stern, D.F.5
  • 21
    • 0013335034 scopus 로고    scopus 로고
    • Gene amplification methods. US patent 5,776,746 (1998)
    • Denney, D. W. Jr Gene amplification methods. US patent 5,776,746 (1998).
    • Denney D.W., Jr.1
  • 22
    • 0033662957 scopus 로고    scopus 로고
    • A mammalian expression vector for expression and purification of secreted proteins for structural studies
    • Leahy, D. J., Dann, C. E., Longo, P., Perman, B. & Ramyar, K. X. A mammalian expression vector for expression and purification of secreted proteins for structural studies. Protein Expr. Purif. 20, 500-506 (2000).
    • (2000) Protein Expr. Purif. , vol.20 , pp. 500-506
    • Leahy, D.J.1    Dann, C.E.2    Longo, P.3    Perman, B.4    Ramyar, K.X.5
  • 23
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 24
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 25
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP an automated program for molecular replacement
    • Vagin, A. & Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025 (1997).
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T., Zou, J.-Y., Cowan, S. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 27
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N. & Murshudov, G. N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D 57, 122-133 (2001).
    • (2001) Acta Crystallogr. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 28
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A. et al. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1
  • 29
  • 30
    • 0026244229 scopus 로고
    • A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.